Interaction between Nonhistone Protein HMGB1 and Linker Histone H1 Facilitates the Formation of Structurally Ordered DNA-Protein Complexes

<table>CD spectra of DNA and its complexes with recombinant protein HMGB1-(AB) at different DNA to protein ratios <svg height="10.325" id="M7" style="vertical-align:-0.0pt" version="1.1" viewbox="0 0 11.6875 10.325" width="11.6875" xmlns="http://www.w3.org/2000/svg">
<g transform="matrix(1.25,0,0,-1.25,0,10.325)">
<g transform="translate(72,-63.74)">
<text transform="matrix(1,0,0,-1,-71.95,63.79)">
<tspan style="font-size: 12.50px; " x="0" y="0">𝑅</tspan>
</text>
</g>
</g>
</svg>, defined as the number of DNA base pairs per one protein molecule in the complex. The complexes with the ratios 45 : 1; 30 : 1; 20 : 1 are marked in the plot. Concentration of DNA in all samples was 0.03 mg/mL; the optical path length was 1.0 cm.</table>

Journal of Spectroscopy

fig2

Figure 2

Figure 2: Interaction between Nonhistone Protein HMGB1 and Linker Histone H1 Facilitates the Formation of Structurally Ordered DNA-Protein Complexes 